Evaluation of immobilization and hydrolytic properties of α-amylase onto chitosan-PVA copolymer
Year: 2025
Type: article
Abstract: The immobilization of α-amylase onto the chitosan-PVA (Chs-co-PVA) copolymer was successfully achieved through physical ad-sorption from its suspension in tris-HCl buffer (0.1 M, pH 8.0, with an activity of 2.89 U/mL). The process resulted in a maximum protein binding efficiency of 79.28% at pH 8.0, with 20.72% of the enzyme remaining unbound. The hydrolysis of starch by both free α-amylase and copolymer-bound α-amylase was evaluated under various reaction conditions. It was found that the immobilized α-amylase exhibited enhanced activity and stability compared to the free enzyme, particularly at elevated temperatures, extended incubation times (50 minutes), and an optimal pH of 8.0. The presence of specific salt ions, including Mg²⁺, Co²⁺, Fe³⁺, Ca²⁺, K⁺, Zn²⁺, Na⁺, Pb²⁺, Hg²⁺, and Cu²⁺, further improved the hydrolytic activity of the immobilized enzyme compared to the free enzyme. Additionally, immobilized α-amylase also demonstrated greater thermo stability, reusability, and storage stability.
DOI: 10.14419/whw2ct15
Authors: Atul, Inderjeet Kaur, Aarti Sharma
Institution: Himachal Pradesh University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
OpenAlex ID: W4409870271